3WUI
Dimeric horse cytochrome c formed by refolding from molten globule state
Summary for 3WUI
Entry DOI | 10.2210/pdb3wui/pdb |
Related | 3WC8 |
Descriptor | Cytochrome c, HEME C, TETRAETHYLENE GLYCOL, ... (6 entities in total) |
Functional Keywords | electron transport |
Biological source | Equus caballus (horse) |
Total number of polymer chains | 1 |
Total formula weight | 12845.54 |
Authors | Deshpande, M.S.,Parui, P.P.,Kamikubo, H.,Yamanaka, M.,Nagao, S.,Komori, H.,Kataoka, M.,Higuchi, Y.,Hirota, S. (deposition date: 2014-04-25, release date: 2014-07-16, Last modification date: 2024-11-20) |
Primary citation | Deshpande, M.S.,Parui, P.P.,Kamikubo, H.,Yamanaka, M.,Nagao, S.,Komori, H.,Kataoka, M.,Higuchi, Y.,Hirota, S. Formation of domain-swapped oligomer of cytochrome C from its molten globule state oligomer. Biochemistry, 53:4696-4703, 2014 Cited by PubMed Abstract: Many proteins, including cytochrome c (cyt c), have been shown to form domain-swapped oligomers, but the factors governing the oligomerization process remain unrevealed. We obtained oligomers of cyt c by refolding cyt c from its acid molten globule state to neutral pH state under high protein and ion concentrations. The amount of oligomeric cyt c obtained depended on the nature of the anion (chaotropic or kosmotropic) in the solution: ClO4(-) (oligomers, 11% ± 2% (heme unit)), SCN(-) (10% ± 2%), I(-) (6% ± 2%), NO3(-) (3% ± 1%), Br(-) (2% ± 1%), Cl(-) (2% ± 1%), and SO4(2-) (3% ± 1%) for refolding of 2 mM cyt c (anion concentration 125 mM). Dimeric cyt c obtained by refolding from the molten globule state exhibited a domain-swapped structure, in which the C-terminal α-helices were exchanged between protomers. According to small-angle X-ray scattering measurements, approximately 25% of the cyt c molecules were dimerized in the molten globule state containing 125 mM ClO4(-). These results indicate that a certain amount of molten globule state oligomers of cyt c convert to domain-swapped oligomers during refolding and that the intermolecular interactions necessary for domain swapping are present in the molten globule state. PubMed: 24981551DOI: 10.1021/bi500497s PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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